ID   NU2M_LEMCA              Reviewed;         347 AA.
AC   Q8LX31;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=NADH-ubiquinone oxidoreductase chain 2 {ECO:0000250|UniProtKB:P03891};
DE            EC=7.1.1.2 {ECO:0000250|UniProtKB:P03891};
DE   AltName: Full=NADH dehydrogenase subunit 2;
GN   Name=MT-ND2 {ECO:0000250|UniProtKB:P03891}; Synonyms=MTND2, NADH2, ND2;
OS   Lemur catta (Ring-tailed lemur).
OG   Mitochondrion.
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Strepsirrhini; Lemuriformes;
OC   Lemuridae; Lemur.
OX   NCBI_TaxID=9447;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12034869; DOI=10.1073/pnas.102164299;
RA   Arnason U., Adegoke J.A., Bodin K., Born E.W., Esa Y.B., Gullberg A.,
RA   Nilsson M., Short R.V., Xu X., Janke A.;
RT   "Mammalian mitogenomic relationships and the root of the eutherian tree.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:8151-8156(2002).
CC   -!- FUNCTION: Core subunit of the mitochondrial membrane respiratory chain
CC       NADH dehydrogenase (Complex I) which catalyzes electron transfer from
CC       NADH through the respiratory chain, using ubiquinone as an electron
CC       acceptor. Essential for the catalytic activity and assembly of complex
CC       I. {ECO:0000250|UniProtKB:P03891}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) +
CC         NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-
CC         COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P03891};
CC   -!- SUBUNIT: Core subunit of respiratory chain NADH dehydrogenase (Complex
CC       I) which is composed of 45 different subunits. Interacts with TMEM242
CC       (By similarity). {ECO:0000250|UniProtKB:P03891,
CC       ECO:0000250|UniProtKB:P03892}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC       {ECO:0000250|UniProtKB:P03892}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the complex I subunit 2 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ421451; CAD13422.1; -; Genomic_DNA.
DR   RefSeq; NP_659289.1; NC_004025.1.
DR   AlphaFoldDB; Q8LX31; -.
DR   SMR; Q8LX31; -.
DR   GeneID; 804955; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005743; C:mitochondrial inner membrane; ISS:UniProtKB.
DR   GO; GO:0070469; C:respirasome; IEA:UniProtKB-KW.
DR   GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; ISS:UniProtKB.
DR   GO; GO:0006120; P:mitochondrial electron transport, NADH to ubiquinone; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   InterPro; IPR010933; NADH_DH_su2_C.
DR   InterPro; IPR003917; NADH_UbQ_OxRdtase_chain2.
DR   InterPro; IPR001750; ND/Mrp_mem.
DR   Pfam; PF06444; NADH_dehy_S2_C; 1.
DR   Pfam; PF00361; Proton_antipo_M; 1.
DR   PRINTS; PR01436; NADHDHGNASE2.
PE   3: Inferred from homology;
KW   Electron transport; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW   NAD; Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW   Transport; Ubiquinone.
FT   CHAIN           1..347
FT                   /note="NADH-ubiquinone oxidoreductase chain 2"
FT                   /id="PRO_0000117600"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        25..45
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        59..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        127..147
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        150..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        323..343
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   347 AA;  39079 MW;  4E6E770554BF927F CRC64;
     MKPIILMFIM LTIFMGTMLT MISSHWLLMW VGLEINMLAI IPILMKKISP RSTEAATKYF
     LTQATASMLL MFSIVINTAN SGQWGITNMH NQLTSLVTMA ALMMKLGMTP FHFWVPEVTQ
     GISLMSGMLL LTWQKLAPIS ILLQIFPSMN PNIILLIAIL SILVGGWGGL NQTQLRKILA
     YSSIAHMGWM MAILMYWPSL TMLNLLIYLM LTITLFSVLN INTNTTTLTL SNTWNKTPMI
     TLTILISLLS LGGLPPLTGF LPKWTIIQEL TKNSNIMLAT IMAIMALLNL YFYMRLIYST
     SLTMFPTLNN MKMKWQFQQT KQIFLLSPLV ILATLTLPLS PALLTLN